Biochemical and immunochemical evidence for the formation of a dimer of glial fibrillary acidic protein.
The glial fibrillary acidic protein isolated from calf brain white matter revealed two major protein bands with apparent molecular weights of 135 000 and 50 000, respectively. The heavy component could be enhanced by oxidation and completely converted to the light component by reduction. It was stoichiometrically established that one sulfhydryl group was present in each 50 000-dalton monomer and the disulfide linkage was involved in dimer formation. The results of the peptide mapping and the immuno-cross-reactivities of the two components indicated that they are identical proteins. We conclude that glial fibrillary acidic protein can occur as a dimeric structure which is formed by an intermolecular disulfide bond from two identical polypeptide chains.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001345:Autoradiography; D001923:Brain Chemistry; D002250:Carbon Radioisotopes; D002417:Cattle; D002531:Cerebellum / Q000032:analysis; D003429:Cross Reactions; D004285:Dogs; D005455:Fluorescent Antibody Technique; D005904:Glial Fibrillary Acidic Protein; D000882:Haplorhini; D005779:Immunodiffusion; D046911:Macromolecular Substances; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000302:isolation & purification*; D013045:Species Specificity
D000596:Amino Acids; D002250:Carbon Radioisotopes; D005904:Glial Fibrillary Acidic Protein; D046911:Macromolecular Substances; D009419:Nerve Tissue Proteins